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Published on: January 14, 2016
Telomeres, histone code, and DNA damage response
1Department of Radiation Oncology, Washington University School of Medicine, St. Louis, MO 63108, USA.
Cytogenetic and Genome Research
|February 4, 2009
Summary
Genomic stability relies on telomeres, protected by unique chromatin structures. This review explores how DNA damage repair proteins, like ATM, and telomere complexes maintain genome integrity through chromatin modifications.
Area of Science:
- Molecular Biology
- Genetics
- Cell Biology
Background:
- Genomic stability is crucial for preventing diseases like cancer.
- Telomeres, the protective caps of chromosomes, are vital for maintaining genomic integrity.
- Altered telomere structure and function are linked to genomic instability and DNA damage response defects.
Purpose of the Study:
- To review the role of DNA damage repair proteins, particularly ATM, in maintaining genomic stability.
- To explore the function of the telomere complex and its associated chromatin structure in genome maintenance.
- To summarize how chromatin modifications influence DNA damage detection and repair pathways at telomeres.
Main Methods:
- Literature review focusing on genomic stability, telomeres, and DNA damage response.
- Analysis of chromatin modifications and their role in histone code.
- Examination of the interplay between ATM, its effectors, and telomere-associated proteins.
Main Results:
- Telomeres possess a unique nucleoprotein structure distinct from DNA double-strand breaks (DSBs).
- Chromatin modifications, governed by a 'histone code,' regulate chromatin accessibility and DSB repair pathway choice.
- Altered telomere chromatin structure is associated with defective DNA damage response (DDR).
Conclusions:
- Chromatin modifying factors are critical for maintaining genomic stability.
- ATM and its effectors, along with the telomere complex, play key roles in genome maintenance.
- Understanding these mechanisms is essential for developing strategies against genomic instability-related diseases.
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In eukaryotic DNA replication, a single-stranded DNA fragment remains at the end of a chromosome after the removal of the final primer. This section of DNA cannot be replicated in the same manner as the rest of the strand because there is no 3’ end to which the newly synthesized DNA can attach. This non-replicated fragment results in gradual loss of the chromosomal DNA during each cell duplication. Additionally, it can induce a DNA damage response by enzymes that recognize single-stranded DNA.
02:41Telomeres and Telomerase
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Overview
02:32Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Acetylation
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02:32Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...